UN112_CAEEL
ID UN112_CAEEL Reviewed; 720 AA.
AC Q18685;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein unc-112;
DE AltName: Full=Mitogen-inducible mig-2 protein-like;
DE AltName: Full=Uncoordinated protein 112;
GN Name=unc-112 {ECO:0000312|WormBase:C47E8.7};
GN ORFNames=C47E8.7 {ECO:0000312|WormBase:C47E8.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF THR-85.
RX PubMed=10893272; DOI=10.1083/jcb.150.1.253;
RA Rogalski T.M., Mullen G.P., Gilbert M.M., Williams B.D., Moerman D.G.;
RT "The UNC-112 gene in Caenorhabditis elegans encodes a novel component of
RT cell-matrix adhesion structures required for integrin localization in the
RT muscle cell membrane.";
RL J. Cell Biol. 150:253-264(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH PAT-4, AND TISSUE SPECIFICITY.
RX PubMed=12015115; DOI=10.1016/s0960-9822(02)00810-2;
RA Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-4/ILK functions as an adaptor protein within integrin
RT adhesion complexes.";
RL Curr. Biol. 12:787-797(2002).
RN [4]
RP SUBUNIT OF A COMPLEX WITH PAT-4 AND PAT-6, AND TISSUE SPECIFICITY.
RX PubMed=12781130; DOI=10.1016/s0960-9822(03)00372-5;
RA Lin X., Qadota H., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-6/actopaxin plays a critical role in the assembly of
RT integrin adhesion complexes in vivo.";
RL Curr. Biol. 13:922-932(2003).
RN [5]
RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-85.
RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471;
RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F.,
RA Jacobson L.A., Szewczyk N.J.;
RT "Calpains mediate integrin attachment complex maintenance of adult muscle
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002471-E1002471(2012).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA Benian G.M.;
RT "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT is required for myofilament stability in Caenorhabditis elegans.";
RL Mol. Biol. Cell 24:601-616(2013).
CC -!- FUNCTION: Component of an integrin containing attachment complex, which
CC is required for muscle development and maintenance (PubMed:22253611).
CC Probable regulator of cell-extracellular matrix adhesion
CC (PubMed:10893272). Required during initial muscle assembly to form
CC dense bodies and M-lines (PubMed:10893272).
CC {ECO:0000269|PubMed:10893272, ECO:0000269|PubMed:22253611}.
CC -!- SUBUNIT: Interacts with pat-4/ILK (PubMed:12015115, PubMed:12781130).
CC Probably forms a complex with pat-4 and pat-6 (PubMed:12781130).
CC Component of an integrin containing attachment complex, composed of at
CC least pat-2, pat-3, pat-4, pat-6, unc-52, unc-97 and unc-112
CC (PubMed:22253611). {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:12781130, ECO:0000305|PubMed:22253611}.
CC -!- INTERACTION:
CC Q18685; Q9TZC4: pat-4; NbExp=5; IntAct=EBI-1564809, EBI-1564527;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10893272};
CC Peripheral membrane protein {ECO:0000269|PubMed:10893272}. Cytoplasm,
CC myofibril, sarcomere, M line {ECO:0000269|PubMed:23283987}.
CC Note=Colocalizes with pat-3/beta-integrin in body wall muscles.
CC Requires unc-52/perlecan and pat-3 to be localized to the muscle cell
CC membrane (PubMed:10893272). Colocalizes with cpna-1 in M line and dense
CC bodies (PubMed:23283987). {ECO:0000269|PubMed:10893272,
CC ECO:0000269|PubMed:23283987}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in muscle cells in both embryos
CC and adults. {ECO:0000269|PubMed:10893272, ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:12781130, ECO:0000269|PubMed:23283987}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in impaired
CC mobility, mitochondrial fragmentation and disrupted integrin attachment
CC complexes in muscle. This leads to degradation of muscle proteins in
CC the cytosol, myofibrillar defects and disruption of sarcomere
CC organization. {ECO:0000269|PubMed:22253611}.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
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DR EMBL; AF217185; AAF20162.1; -; mRNA.
DR EMBL; BX284605; CAA99790.1; -; Genomic_DNA.
DR PIR; T20016; T20016.
DR RefSeq; NP_506628.1; NM_074227.6.
DR AlphaFoldDB; Q18685; -.
DR SMR; Q18685; -.
DR BioGRID; 44974; 6.
DR IntAct; Q18685; 2.
DR STRING; 6239.C47E8.7.1; -.
DR iPTMnet; Q18685; -.
DR EPD; Q18685; -.
DR PaxDb; Q18685; -.
DR PeptideAtlas; Q18685; -.
DR EnsemblMetazoa; C47E8.7.1; C47E8.7.1; WBGene00006836.
DR GeneID; 179972; -.
DR KEGG; cel:CELE_C47E8.7; -.
DR UCSC; C47E8.7.1; c. elegans.
DR CTD; 179972; -.
DR WormBase; C47E8.7; CE05443; WBGene00006836; unc-112.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_0_0_1; -.
DR InParanoid; Q18685; -.
DR OMA; EDQYARW; -.
DR OrthoDB; 248494at2759; -.
DR PhylomeDB; Q18685; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-446353; Cell-extracellular matrix interactions.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q18685; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006836; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030055; C:cell-substrate junction; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:WormBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IMP:UniProtKB.
DR GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IDA:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:1904901; P:positive regulation of myosin II filament organization; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:1901074; P:regulation of engulfment of apoptotic cell; IMP:WormBase.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; PTHR16160; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..720
FT /note="Protein unc-112"
FT /id="PRO_0000219458"
FT DOMAIN 288..614
FT /note="FERM"
FT DOMAIN 402..507
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 145..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85
FT /note="T->I: In R367; temperature sensitive. Adults are
FT paralyzed. Induces disorganized body wall muscle. Disrupted
FT integrin attachment complexes in muscle, which results in
FT degradation of muscle proteins in the cytosol, myofibrillar
FT defects and disruption of sarcomere organization.
FT Mitochondrial fragmentation."
FT /evidence="ECO:0000269|PubMed:10893272,
FT ECO:0000269|PubMed:22253611"
SQ SEQUENCE 720 AA; 82355 MW; 663CB0E9891C1A12 CRC64;
MAHLVEGTSI IDGKWQLPIL VTDLNIQRSI SVLGNLNVGG LMLELVSECD VERDWSDHAL
WWPEKRRWLQ HTRSTLDQNG ITAETQLEFT PMHKEARIQL PDMQMIDARV DFSVNSFKAT
KKLCRDLGIR YSEELSLKRY IPPEDLRRGT SDADNMNGPL SMRPGEESVG PMTLRKAAPI
FASQSNLDMR RRGQSPALSQ SGHIFNAHEM GTLPRHGTLP RGVSPSPGAY NDTMRRTPIM
PSISFSEGLE NEQFDDALIH SPRLAPSRDT PVFRPQNYVE KAAINRGWLD SSRSLMEQGI
FEGDIILLRF KFMNFFDLNP KYDPVRINQL YEQAKWSILL DEFDHTEEEA TLFAALQLQA
TLQRDSPEPE ENNKDDVDIL LDELEQNLDA AALNRRSDLT QVPELADYLK YMKPKKLAAF
KGFKRAFFSF RDLYLSYHQS SSDVNSAPLG HFSLKGCEVS QDVSVGQQKY HIKLLLPTAE
GMIDFILKCD SEHQYARWMA ACRLASRGKS MADSSYQQEV ESIKNLLKMQ SGNGNENGNS
NTASRKAAAV KLPNDFNVDE YISSKYVRRA RSKQQIQQRV SDAHGNVRQL TATEAKLQYI
RAWQALPEHG IHYFIVRFRN ARKAELVAVA VNRLAKLNMD NGESLKTWRF ANMKKWHVNW
EIRHLKIQFE DEDIEFKPLS ADCKVVHEFI GGYIFLSMRS KEHSQNLDEE LFHKLTGGWA
